ID D4G8G6_RIEPU Unreviewed; 244 AA.
AC D4G8G6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|ARBA:ARBA00016139, ECO:0000256|RuleBase:RU361267};
DE EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN OrderedLocusNames=RIEPE_0378 {ECO:0000313|EMBL:ADD79697.1};
OS Riesia pediculicola (strain USDA).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Riesia.
OX NCBI_TaxID=515618 {ECO:0000313|EMBL:ADD79697.1, ECO:0000313|Proteomes:UP000001700};
RN [1] {ECO:0000313|EMBL:ADD79697.1, ECO:0000313|Proteomes:UP000001700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USDA {ECO:0000313|EMBL:ADD79697.1,
RC ECO:0000313|Proteomes:UP000001700};
RA Kirkness E.F.;
RT "Genome sequence of Riesia pediculicola USDA.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC Evidence={ECO:0000256|ARBA:ARBA00001141,
CC ECO:0000256|RuleBase:RU361267};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000256|RuleBase:RU361267}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC ECO:0000256|RuleBase:RU361267}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001085; ADD79697.1; -; Genomic_DNA.
DR AlphaFoldDB; D4G8G6; -.
DR STRING; 515618.RIEPE_0378; -.
DR KEGG; rip:RIEPE_0378; -.
DR eggNOG; COG0204; Bacteria.
DR HOGENOM; CLU_027938_10_3_6; -.
DR OrthoDB; 5290997at2; -.
DR UniPathway; UPA00557; UER00613.
DR Proteomes; UP000001700; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR004552; AGP_acyltrans.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW ECO:0000313|EMBL:ADD79697.1};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:ADD79697.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..184
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 244 AA; 28618 MW; B264445D75729C14 CRC64;
MLAIFRIIFL FFSFFLICLF GIFNCVVRPK CLQHTFLLGK LFGRLSKILG VKVIVRISKK
SKELMKLPSI YIGNHQSFYD IFTISNAIQP YTVTVGKKNL IFIPIFGQLY WLCGNVLLDR
KNRDQIRKSI LKIIRYIRNQ GRSVWIFPEG TRNKGKNLLP FKNGAFRIAK ISRVPIIPIC
SSEISRKIRL NRWRNGTVII EILDPIFIED QKYDKRSLTC LKKFCFNLMK KKIFSLNQEI
KKSN
//
